Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2PPF

Reduced mutant D98N of AfNiR exposed to nitric oxide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005507	molecular_function	copper ion binding
A	0016491	molecular_function	oxidoreductase activity
A	0019333	biological_process	denitrification pathway
A	0042128	biological_process	nitrate assimilation
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding
A	0050421	molecular_function	nitrite reductase (NO-forming) activity
B	0005507	molecular_function	copper ion binding
B	0016491	molecular_function	oxidoreductase activity
B	0019333	biological_process	denitrification pathway
B	0042128	biological_process	nitrate assimilation
B	0042597	cellular_component	periplasmic space
B	0046872	molecular_function	metal ion binding
B	0050421	molecular_function	nitrite reductase (NO-forming) activity
C	0005507	molecular_function	copper ion binding
C	0016491	molecular_function	oxidoreductase activity
C	0019333	biological_process	denitrification pathway
C	0042128	biological_process	nitrate assimilation
C	0042597	cellular_component	periplasmic space
C	0046872	molecular_function	metal ion binding
C	0050421	molecular_function	nitrite reductase (NO-forming) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU1 A 501

Chain	Residue
A	HIS95
A	CYS136
A	HIS145
A	MET150

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 502

Chain	Residue
A	HIS100
A	HIS135
A	NO1511
B	HIS306

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU1 B 501

Chain	Residue
B	CYS136
B	HIS145
B	MET150
B	CU1504
B	HIS95

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU B 502

Chain	Residue
B	HIS100
B	HIS135
B	NO503
C	HIS306

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU1 C 501

Chain	Residue
C	HIS95
C	CYS136
C	HIS145
C	MET150
C	CU1504

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU C 502

Chain	Residue
A	HIS306
A	NO503
C	HIS100
C	HIS135
C	NO505

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU1 B 504

Chain	Residue
B	CYS136
B	PRO138
B	HIS145
B	CU1501

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU1 C 504

Chain	Residue
C	CYS136
C	PRO138
C	HIS145
C	CU1501

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT B 1503

Chain	Residue
B	THR228
B	GLY229
B	HIS319
B	HOH1829

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT B 1504

Chain	Residue
A	GLU113
A	HOH1547
B	ASP173
B	GLY238
B	GLU239
B	LYS240
B	HOH1587

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT B 1505

Chain	Residue
B	GLY140
B	MET141
B	VAL142
B	PRO143
B	TRP144
B	MET210
C	GLU313

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT B 1506

Chain	Residue
A	HOH1670
B	PHE282
B	HOH1516
B	HOH1678
B	HOH1681
C	PHE282
C	HOH1643

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT C 1507

Chain	Residue
C	VAL59
C	HIS60
C	TYR184
C	THR206
C	HOH1539
C	HOH1623
C	HOH1630

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT C 1508

Chain	Residue
A	GLU313
C	GLY140
C	MET141
C	VAL142
C	PRO143
C	TRP144

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT C 1509

Chain	Residue
C	THR228
C	GLY229
C	ILE300
C	HIS319
C	LYS321

site_id	BC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ACT A 1510

Chain	Residue
A	GLY140
A	MET141
A	VAL142
A	PRO143
A	TRP144
A	TYR203
A	VAL207
B	GLU313
B	GLU325

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NO A 503

Chain	Residue
A	ILE257
A	HIS306
C	HIS135
C	CU502
C	NO505

site_id	BC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NO C 505

Chain	Residue
A	ILE257
A	HIS306
A	NO503
C	HIS100
C	HIS135
C	CU502
C	HOH1510

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NO A 1511

Chain	Residue
A	HIS100
A	HIS135
A	CU502
A	HOH1512
B	ILE257
B	HIS306

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NO B 503

Chain	Residue
B	HIS100
B	HIS135
B	CU502
B	HOH1849
C	ILE257
C	HIS306

site_id	CC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TRS B 1501

Chain	Residue
A	THR212
A	LEU213
A	THR214
B	THR212
B	LEU213
B	THR214
B	HOH1513
B	HOH1669
C	THR212
C	LEU213
C	THR214

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: type 1 copper site => ECO:0000269\|PubMed:8172899

Chain	Residue	Details
A	HIS95
B	HIS95
C	HIS95

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: type 2 copper site

Chain	Residue	Details
A	HIS100
A	HIS135
B	HIS100
B	HIS135
C	HIS100
C	HIS135

site_id	SWS_FT_FI3
Number of Residues	9
Details	BINDING: type 1 copper site

Chain	Residue	Details
A	CYS136
A	HIS145
A	MET150
B	CYS136
B	HIS145
B	MET150
C	CYS136
C	HIS145
C	MET150

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: type 2 copper site => ECO:0000269\|PubMed:8172899

Chain	Residue	Details
A	HIS306
B	HIS306
C	HIS306

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
A	ASN98
A	HIS255

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
B	ASN98
B	HIS255

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
C	ASN98
C	HIS255

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)